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Properties of the 47KDa Protein and the D1-D2-Cyt B559 Complex

  • D. F. Ghanotakis
  • G. T. Babcock
  • C. F. Yocum
Part of the NATO ASI Series book series (NSSA, volume 168)

Abstract

In the present paper we describe a new method for the isolation of the 47 kDa protein and the D1-D2-Cyt b559 complex that uses the non-ionic detergent dodecylmaltoside in combination with high concentrations of lithium Perchlorate to dissociate polypeptides of the PSII complex, followed by FPLC ion-exchange chromatography to separate these polypeptides. By carrying out a low temperature EPR study of the two systems we support the proposal that the D1-D2 complex, and not the 47 kDa polypeptide, is the species which binds the reaction center öf PSII. The EPR signal from the spin-polarized triplet was also used as a probe of the stability of the D1-D2-Cyt b559 preparation. It was found that more than 80% of the EPR signal intensity from the spin-polarized triplet could still be observed after incubation of our D1-D2-Cyt b559 complex in the dark at room temperature for five hours.

Keywords

B559 Complex Lithium Perchlorate Reaction Center Complex PSII Membrane Room Temperature Absorption Spectrum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • D. F. Ghanotakis
    • 1
  • G. T. Babcock
    • 2
  • C. F. Yocum
    • 3
  1. 1.Department of ChemistryUniversity of Crete IraklionCreteGreece
  2. 2.Department of ChemistryMichigan State UniversityEast LansingUSA
  3. 3.Departments of Biology and ChemistryThe University of MichiganAnn ArborUSA

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